Journal of the American Chemical Society, Vol.121, No.50, 11813-11820, 1999
Surface recognition and helix stabilization of a tetraaspartate peptide by shape and electrostatic complementarity of an artificial receptor
The recognition of tetraaspartate peptide (2) by tetra-guanidinium (1) in (a) water and (b) aqueous methanol (10% H2O/90% CH3OH) has been investigated. The conformations of the free peptide and its complex with 1 have been characterized in both solvent systems by CD and 2D NMR spectroscopies. Increased alpha-helicity as a result of solvent composition and receptor binding are discussed. Control experiments show that the recognition stems from complementary electrostatic interactions, hydrogen bonding, and matching of surface topologies.